H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH contains dual cysteines capable of disulfide stabilization, influencing tertiary structure formation. Charged and aromatic residues provide a diverse environment for binding studies. Researchers investigate its folding dynamics and structural preferences. Applications span sequence engineering, motif characterization, and receptor-interaction modeling.
CAT No: R2635
CAS No:1876450-21-3
Synonyms/Alias:H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH;MM 07;1876450-21-3;MM07;CHEMBL4475589;H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH;MM 07 TFA;cyclo[1-6]CRPRLCHKGPMPF;GTPL8523;BAD45021;BDBM50518047;MM 07?;DA-55564;HY-108003;CS-0027130;G16472;L-cysteinyl-L-arginyl-L-prolyl-L-arginyl-L-leucyl-L-cysteinyl-L-histidyl-L-lysyl-glycyl-L-prolyl-L-methionyl-L-prolyl-L-phenylalanine (1->6)-disulfide;
H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH is a specialized synthetic peptide designed for advanced research applications in the fields of biochemistry and molecular biology. Characterized by its unique amino acid sequence, this peptide offers a valuable tool for scientists exploring protein-protein interactions, structural biology, and signal transduction pathways. Its distinct arrangement, including the presence of cysteine residues at specific positions, allows for potential disulfide bridge formation, which can be critical in studies of peptide folding and stability. The sequence also incorporates charged and hydrophobic residues, enabling diverse interactions with biological targets and facilitating investigations into peptide binding mechanisms and conformational dynamics.
Protein-Protein Interaction Studies: H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH serves as a model system for examining the intricacies of protein-protein interactions. Researchers utilize this peptide to mimic specific motifs found in natural proteins, enabling the dissection of binding sites and interaction domains. By introducing the peptide into in vitro assays, scientists can monitor how it associates with target proteins, map critical contact points, and elucidate the structural determinants that govern complex formation. Such studies are instrumental in understanding the molecular basis of cellular signaling and regulatory mechanisms.
Peptide Folding and Stability Research: The sequence's two cysteine residues provide an opportunity to investigate disulfide bond formation and its impact on peptide structure. In folding studies, this compound is used to probe how covalent linkages influence secondary and tertiary structure stabilization. Researchers can employ various spectroscopic and chromatographic techniques to monitor folding kinetics, thermodynamic stability, and conformational changes. Insights gained from these experiments contribute to a deeper understanding of protein folding diseases and the fundamental principles governing peptide architecture.
Signal Transduction Pathway Analysis: By integrating the peptide into cellular or biochemical models, scientists can explore its role as a modulator or mimic of endogenous signaling peptides. The basic and hydrophobic residues within the sequence enable interactions with membrane components or intracellular signaling proteins, making it a useful tool for dissecting pathways involved in cell communication and response. Experimental approaches may include phosphorylation assays, binding studies, and functional analyses to determine how the peptide influences downstream signaling events.
Enzyme Substrate and Inhibitor Design: H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH is frequently employed in the design and characterization of enzyme substrates or inhibitors. By serving as a template, it assists researchers in identifying key sequence features required for enzymatic recognition and catalysis. Modification of specific residues within the peptide can yield variants with altered substrate specificity or inhibitory potency, aiding in the development of novel biochemical tools for probing enzyme function and regulation.
Structural Biology and Spectroscopy: The distinct sequence of this peptide makes it an excellent candidate for structural studies using NMR, X-ray crystallography, or circular dichroism spectroscopy. These techniques allow scientists to resolve its three-dimensional conformation, assess dynamic properties, and compare experimental data with computational models. Such investigations not only provide atomic-level insights into peptide structure but also inform the design of analogs with tailored properties for specific research objectives. Peptides like H-Cys(1)-Arg-Pro-Arg-Leu-Cys(1)-His-Lys-Gly-Pro-Met-Pro-Phe-OH continue to play a pivotal role in advancing our understanding of molecular interactions, structural principles, and functional mechanisms in the life sciences.
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